O34522 (TRMB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
tRNA (guanine-N(7)-)-methyltransferase
EC=2.1.1.33

Alternative name(s):
BsTrmB
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase

Gene names

Name:	trmB
Synonyms:	ytmQ
Ordered Locus Names:	BSU29900

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. HAMAP-Rule MF_01057
Catalytic activity	S-adenosyl-L-methionine + guanine46 in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine46 in tRNA. Ref.3
Pathway	tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP-Rule MF_01057
Sequence similarities	Belongs to the methyltransferase superfamily. TrmB family.

Ontologies

Keywords
Biological process	tRNA processing
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA (guanine-N7)-methylation Inferred from electronic annotation. Source: GOC
Molecular_function	tRNA (guanine-N7-)-methyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 213

213

tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057

PRO_0000171295

Regions

Region

124 – 129

6

Interaction with RNA Potential

Region

191 – 194

4

Substrate binding Potential

Sites

Binding site

44

1

S-adenosyl-L-methionine By similarity

Binding site

69

1

S-adenosyl-L-methionine By similarity

Binding site

96

1

S-adenosyl-L-methionine By similarity

Binding site

118

1

S-adenosyl-L-methionine By similarity

Binding site

122

1

Substrate By similarity

Binding site

154

1

Substrate Potential

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

213

Helix Strand Turn

Details...

Helix

10 – 15

6

Turn

16 – 19

4

Helix

24 – 27

4

Helix

31 – 35

5

Beta strand

41 – 45

5

Helix

51 – 59

9

Beta strand

63 – 68

6

Helix

72 – 84

13

Beta strand

88 – 93

6

Helix

97 – 99

3

Helix

100 – 103

4

Beta strand

111 – 116

6

Helix

123 – 128

6

Helix

133 – 143

11

Beta strand

148 – 154

7

Helix

156 – 169

14

Beta strand

172 – 179

8

Helix

180 – 182

3

Helix

194 – 196

3

Beta strand

197 – 201

5

Beta strand

205 – 210

6

Sequences

	Sequence		Length	Mass (Da)
	O34522 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 28C34F163EB2DD69	FASTA	213	24,504
	10 20 30 40 50 60 MRMRHKPWAD DFLAENADIA ISNPADYKGK WNTVFGNDNP IHIEVGTGKG QFISGMAKQN 70 80 90 100 110 120 PDINYIGIEL FKSVIVTAVQ KVKDSEAQNV KLLNIDADTL TDVFEPGEVK RVYLNFSDPW 130 140 150 160 170 180 PKKRHEKRRL TYSHFLKKYE EVMGKGGSIH FKTDNRGLFE YSLKSFSEYG LLLTYVSLDL 190 200 210 HNSNLEGNIM TEYEEKFSAL GQPIYRAEVE WRT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region." Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Crystal structure of Bacillus subtilis TrmB, the tRNA (m7G46) methyltransferase." Zegers I., Gigot D., van Vliet F., Tricot C., Aymerich S., Bujnicki J.M., Kosinski J., Droogmans L. Nucleic Acids Res. 34:1925-1934(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), CATALYTIC ACTIVITY. Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF008220 Genomic DNA. Translation: AAC00285.1.
AL009126 Genomic DNA. Translation: CAB14968.1.

PIR

B69997.

RefSeq

NP_390868.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FCA	X-ray	2.10	A/B	1-213	[»]

ProteinModelPortal

O34522.

SMR

O34522. Positions 10-213.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU29900.

Proteomic databases

PaxDb

O34522.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB14968; CAB14968; BSU29900.

GeneID

936447.

KEGG

bsu:BSU29900.

PATRIC

18977886. VBIBacSub10457_3131.

Organism-specific databases

GenoList

BSU29900. [Micado]

Phylogenomic databases

eggNOG

COG0220.

HOGENOM

HOG000251689.

KO

K03439.

OMA

RLRNKPW.

ProtClustDB

PRK00121.

Enzyme and pathway databases

BioCyc

BSUB:BSU29900-MONOMER.

UniPathway

UPA00989.

Family and domain databases

HAMAP

MF_01057. tRNA_methyltr_TrmB.

InterPro

IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]

Pfam

PF02390. Methyltransf_4. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00091. TIGR00091. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O34522.

Entry information

Entry name

TRMB_BACSU

Accession

Primary (citable) accession number: O34522

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program